In an effort to identify a microbial lipase that can catalyze transesterification reactions used in biodiesel production, an organic solvent-tolerant lipase was purified from Streptomyces sp. CS268. The molecular weight of the purified lipase was estimated to be 37.5 kDa by SDS-PAGE. The lipase showed highest activity at a temperature of $30^{circ}C$ and pH 8.0 while it was stable in the pH range 4.0 ~ 9.0 and at temperatures ${leq}50^{circ}C$. It showed the highest hydrolytic activity towards medium-length acyl chain p-nitrophenyl decanoate with $K_m$ and $V_{max}$ values of 0.59 mM and 319.5 mmol/mg/min, respectively. Also, the lipase showed non-position specificity for triolein hydrolysis. The purified lipase catalyzed transesterification reaction of soybean oil with methanol, suggesting that it can be a potential enzymatic catalyst for biodiesel production.